› 6a1t

X-ray diffraction
1.97Å resolution

Charcot-Leyden crystal protein/Galectin-10 variant E33A with lactose

Released:
DOI: 10.2210/pdb6a1t/pdb
PDB entry 6a1t coloured by chain, front view.
PDB entry 6a1t coloured by chain, side view.
PDB entry 6a1t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of key amino acid residues determining ligand binding specificity, homodimerization and cellular distribution of human galectin-10.
Su J, Song C, Si Y, Cui L, Yang T, Li Y, Wang H, Tai G, Zhou Y
Glycobiology 29 85-93 (2019)
PMID: 30239701

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170169 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Galectin-10 Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05315 (Residues: 1-142; Coverage: 100%)
Gene names: CLC, LGALS10, LGALS10A
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P6522
Unit cell:
a: 48.944Å b: 48.944Å c: 262.43Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.188 0.23
Expression system: Escherichia coli

Quick links

Citations

4 review citations

A Brief History of Charcot-Leyden Crystal Protein/Galectin-10 Research.
Su J. (2018)
3 more

1 mention without citation

The Structural Biology of Galectin-Ligand Recognition: Current Advances in Modeling Tools, Protein Engineering, and Inhibitor Design.
Modenutti et al. (2019)